The distance geometry approach to conformatonal calculations has been very successful in producing conformations satisfying strictly geometric constraints, but there has been no way to weight the constraints or to include energetic considerations. I propose to develop an extension of distance geometry that not only handles geometric constraints, but also produces low energy conformations. Among the numerous applications for such a technique, I am particuarly interested in studying protein folding, which is of course central to the basic understanding of molecular biology. My preliminary results indicate that the energy embedding extension to distance geometry deals with geometic constraints as successfully as always, and also produces conformers of very low energy. The results further indicate that the first goal should be an improved polypeptide energy function to use in conjunction with the method. Clearly the prediction of protein structure from sequence alone would be of immense importance in biochemistry. However, even much more limited success at deducing energeticaly plausible solution conformations of large molecules given experimental data insufficient to fully determine the stru cture, could be a great aid to a wide audience of experimentalists. Such applications allow one to test how good the potential function really is, to deduce the most crucial further experiments for determining conformation, and to discover alternate conformers that also agree with the evidence.